B. Berks

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A common export pathway for proteins binding complex redox cofactors?

B. Berks, 1996, Molecular microbiology.

The TatA component of the twin-arginine protein transport system forms channel complexes of variable diameter.

Helen R Saibil, Tracy Palmer, H. Saibil, 2005, Proceedings of the National Academy of Sciences of the United States of America.

The twin-arginine translocation (Tat) protein export pathway

Tracy Palmer, B. Berks, T. Palmer, 2012, Nature Reviews Microbiology.

Structure of the TatC core of the twin-arginine protein transport system

C. Robinson, B. Berks, P. Roversi, 2012, Nature.

Characterization and membrane assembly of the TatA component of the Escherichia coli twin-arginine protein transport system.

B. Wallace, B. Berks, R. Wallis, 2002, Biochemistry.

The twin-arginine protein translocation pathway.

B. Berks, 2015, Annual review of biochemistry.

Precursor–Receptor Interactions in the Twin Arginine Protein Transport Pathway Probed with a New Receptor Complex Preparation

C. Robinson, B. Berks, J. Gault, 2018, Biochemistry.

Structures of the Type IX Secretion/Gliding Motility Motor from across the Phylum Bacteroidetes

B. Berks, S. Lea, J. Deme, 2022, mBio.

Control of periplasmic nitrate reductase gene expression (napEDABC) from Paracoccus pantotrophus in response to oxygen and carbon substrates.

G. Sawers, D. Richardson, B. Berks, 2000, Microbiology.

MicroReview The Tat protein export pathway

B. Berks, T. Palmer, F. Sargent, 2000 .

Mo(V) co-ordination in the periplasmic nitrate reductase from Paracoccus pantotrophus probed by electron nuclear double resonance (ENDOR) spectroscopy.

D. Richardson, B. Berks, S. Fairhurst, 2002, The Biochemical journal.

Mechanism for the Hydrolysis of a Sulfur-Sulfur Bond Based on the Crystal Structure of the Thiosulfohydrolase SoxB*

E. Garman, B. Berks, P. Roversi, 2009, The Journal of Biological Chemistry.

Mo(V) electron paramagnetic resonance signals from the periplasmic nitrate reductase of Thiosphaera pantotropha.

D. Richardson, B. Berks, A. Thomson, 1994, European journal of biochemistry.

Isolation and structural characterization of insulin and glucagon from the holocephalan species Callorhynchus milii (elephantfish).

B. Berks, C. Marshall, A. Carne, 1989, The Biochemical journal.

A complex iron-calcium cofactor catalyzing phosphotransfer chemistry

E. Garman, B. Berks, P. Roversi, 2014, Science.

Redox and Chemical Activities of the Hemes in the Sulfur Oxidation Pathway Enzyme SoxAX*

B. Berks, A. Hemmings, J. Butt, 2012, The Journal of Biological Chemistry.

Formation of a cytochrome c-nitrous oxide reductase complex is obligatory for N2O reduction by Paracoccus pantotrophus.

B. Berks, T. Rasmussen, A. Thomson, 2005, Dalton transactions.

Multiple forms of the catalytic centre, CuZ, in the enzyme nitrous oxide reductase from Paracoccus pantotrophus.

B. Berks, T. Rasmussen, A. Thomson, 2002, The Biochemical journal.

Specificity of respiratory pathways involved in the reduction of sulfur compounds by Salmonella enterica.

B. Berks, A. Hinsley, 2002, Microbiology.

Structures of the Type IX Secretion/Gliding Motility Motor from across the Phylum Bacteroidetes

B. Berks, S. Lea, J. Deme, 2022, bioRxiv.

Cysteine Scanning Mutagenesis and Topological Mapping of the Escherichia coli Twin-Arginine Translocase TatC Component

B. Berks, C. Punginelli, T. Palmer, 2007, Journal of bacteriology.

Formation of functional Tat translocases from heterologous components

B. Berks, T. Palmer, I. Caldelari, 2006, BMC Microbiology.

The catalytic center in nitrous oxide reductase, CuZ, is a copper-sulfide cluster.

B. Berks, D. Dooley, T. Rasmussen, 2000, Biochemistry.

Biochemistry: Cells enforce an ion curtain

B. Berks, 2008, Nature.

Crystallization and preliminary X-ray analysis of nitrous oxide reductase from Paracoccus pantotrophus.

V. Fülöp, B. Berks, S. Ferguson, 2000, Acta crystallographica. Section D, Biological crystallography.

The TatC component of the twin‐arginine protein translocase functions as an obligate oligomer

B. Berks, P. Stansfeld, M. Wallace, 2015, Molecular microbiology.

The DNA transporter ComEC has metal‐dependent nuclease activity that is important for natural transformation

B. Berks, S. Lea, Augustinas Silale, 2021, Molecular microbiology.

SoxV, an orthologue of the CcdA disulfide transporter, is involved in thiosulfate oxidation in Rhodovulum sulfidophilum and reduces the periplasmic thioredoxin SoxW.

B. Berks, C. Appia-Ayme, 2002, Biochemical and biophysical research communications.

Protein voltammetry and spectroscopy: integrating approaches

B. Berks, L. Male, J. Butt, 2008 .

TatBC, TatB, and TatC form structurally autonomous units within the twin arginine protein transport system of Escherichia coli

B. Berks, M. Tarry, T. Palmer, 2007, FEBS letters.

Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions.

D. Richardson, B. Berks, S. Ferguson, 1995, Biochimica et biophysica acta.

Thiocyanate binding to the molybdenum centre of the periplasmic nitrate reductase from Paracoccus pantotrophus.

D. Richardson, B. Berks, A. Thomson, 2000, The Biochemical journal.

Mo(V) co-ordination in the periplasmic nitrate reductase from Paracoccus pantotrophus probed by electron nuclear double resonance (ENDOR) spectroscopy

D. Richardson, B. Berks, S. Fairhurst, 2002 .

Assignment of haem ligands and detection of electronic absorption bands of molybdenum in the di‐haem periplasmic nitrate reductase of Paracoccus pantotrophus

D. Richardson, B. Berks, A. Thomson, 2001, FEBS letters.

The Tat Protein Export Pathway

B. Berks, T. Palmer, F. Sargent, 2010, EcoSal Plus.

The Twin-Arginine Transport System

B. Berks, T. Palmer, F. Sargent, 2005 .

Assembly of membrane-bound respiratory complexes by the Tat protein-transport system

B. Berks, T. Palmer, F. Sargent, 2002, Archives of Microbiology.

Models for molybdenum coordination during the catalytic cycle of periplasmic nitrate reductase from Paracoccus denitrificans derived from EPR and EXAFS spectroscopy.

D. Richardson, B. Berks, A. Thomson, 1999, Biochemistry.

Spectroscopic Characterization of a Novel Multihemec-Type Cytochrome Widely Implicated in Bacterial Electron Transport*

D. Richardson, B. Berks, A. Thomson, 1998, The Journal of Biological Chemistry.

Identification of an assimilatory nitrate reductase in mutants of Paracoccus denitrificans GB17 deficient in nitrate respiration

D. Richardson, B. Berks, S. Ferguson, 1997, Archives of Microbiology.

The napEDABC gene cluster encoding the periplasmic nitrate reductase system of Thiosphaera pantotropha.

D. Richardson, B. Berks, S. Ferguson, 1995, The Biochemical journal.

Characterization of the paramagnetic iron‐containing redox centres of Thiosphaera pantotropha periplasmic nitrate reductase

D. Richardson, B. Berks, A. Thomson, 1994, FEBS letters.

Purification and characterization of the periplasmic nitrate reductase from Thiosphaera pantotropha.

C. Robinson, D. Richardson, B. Berks, 1994, European journal of biochemistry.

The bacterial nitrate reductases

D. Richardson, B. Berks, S. Ferguson, 1998 .

The Tat protein export pathway

B. Berks, T. Palmer, F. Sargent, 2000, Molecular microbiology.

Functional, biochemical and genetic diversity of prokaryotic nitrate reductases

D. A. Russell, D. Russell, D. Richardson, 2001, Cellular and Molecular Life Sciences CMLS.

Insertion of transposon Tn5 into a structural gene of the membrane-bound nitrate reductase of Thiosphaera pantotropha results in anaerobic overexpression of periplasmic nitrate reductase activity.

D. Richardson, B. Berks, M. D. Page, 1993, Journal of general microbiology.

Sec-independent Protein Translocation in Escherichia coli

B. Berks, T. Palmer, F. Sargent, 1999, The Journal of Biological Chemistry.

Overlapping functions of components of a bacterial Sec‐independent protein export pathway

B. Berks, T. Palmer, F. Sargent, 1998, The EMBO journal.

A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system.

M. Quail, J. McClay, J. McClay, 1997, Microbiology.

The SoxYZ Complex Carries Sulfur Cycle Intermediates on a Peptide Swinging Arm*

B. Berks, A. Hemmings, V. Sauvé, 2007, Journal of Biological Chemistry.

Cytochrome Complex Essential for Photosynthetic Oxidation of both Thiosulfate and Sulfide in Rhodovulum sulfidophilum

B. Berks, A. Leech, C. Appia-Ayme, 2001, Journal of bacteriology.

The Tat protein translocation pathway and its role in microbial physiology.

Frank Sargent, Tracy Palmer, B. Berks, 2003, Advances in microbial physiology.

Structure and mechanism of the proton-driven motor that powers Type 9 secretion and gliding motility

B. Berks, Steven Johnson, S. Lea, 2020, Nature Microbiology.

Type 9 secretion system structures reveal a new protein transport mechanism

B. Berks, S. Lea, J. Deme, 2018, Nature.

Live cell imaging shows reversible assembly of the TatA component of the twin-arginine protein transport system

B. Berks, M. Wallace, T. Palmer, 2013, Proceedings of the National Academy of Sciences.

Processing by rhomboid protease is required for Providencia stuartii TatA to interact with TatC and to form functional homo-oligomeric complexes

B. Berks, M. Tarry, T. Palmer, 2012, Molecular microbiology.

Escherichia coli Strains Blocked in Tat-Dependent Protein Export Exhibit Pleiotropic Defects in the Cell Envelope

B. Berks, T. Palmer, K. Findlay, 2001, Journal of bacteriology.

Protein targeting by the bacterial twin-arginine translocation (Tat) pathway.

Frank Sargent, Tracy Palmer, B. Berks, 2005, Current opinion in microbiology.

Identification of two domains and distal histidine ligands to the four haems in the bacterial c-type cytochrome NapC; the prototype connector between quinol/quinone and periplasmic oxido-reductases.

D. Richardson, B. Berks, S. Ferguson, 2002, The Biochemical journal.

Moving folded proteins across the bacterial cell membrane.

B. Berks, T. Palmer, 2003, Microbiology.

A signal sequence suppressor mutant that stabilizes an assembled state of the twin arginine translocase

B. Berks, T. Palmer, Sarah E. Rollauer, 2017, Proceedings of the National Academy of Sciences.

Structural basis for specificity and promiscuity in a carrier protein/enzyme system from the sulfur cycle

B. Berks, Steven Johnson, S. Lea, 2015, Proceedings of the National Academy of Sciences.

Structural basis for the oxidation of thiosulfate by a sulfur cycle enzyme

Stefano Bruno, B. Berks, A. Hemmings, 2002, The EMBO journal.

TatD Is a Cytoplasmic Protein with DNase Activity

B. Berks, T. Palmer, F. Sargent, 2000, The Journal of Biological Chemistry.

Behaviour of topological marker proteins targeted to the Tat protein transport pathway

Frank Sargent, Tracy Palmer, Grant Buchanan, 2002, Molecular microbiology.

Intermediates in the Sox sulfur oxidation pathway are bound to a sulfane conjugate of the carrier protein SoxYZ

B. Berks, D. B. Grabarczyk, 2017, PloS one.

Membrane-associated NADH dehydrogenase activities in Rhodobacter capsulatus: purification of a dihydrolipoyl dehydrogenase.

A. McEwan, B. Berks, S. Ferguson, 1993, Journal of general microbiology.

Characterisation and amino acid sequence of cytochrome c-550 from Thiosphaera pantotropha.

J. V. Van Beeumen, B. Berks, M. D. Page, 1994, European journal of biochemistry.

Sequence and expression of the gene encoding the respiratory nitrous-oxide reductase from Paracoccus denitrificans. New and conserved structural and regulatory motifs.

B. Berks, J. McCarthy, S. Ferguson, 1993, European journal of biochemistry.

Pathfinders and trailblazers: a prokaryotic targeting system for transport of folded proteins.

B. Berks, T. Palmer, F. Sargent, 2006, FEMS microbiology letters.

The Twin Arginine Consensus Motif of Tat Signal Peptides Is Involved in Sec-independent Protein Targeting in Escherichia coli *

B. Berks, T. Palmer, N. Stanley, 2000, The Journal of Biological Chemistry.

mRNA Secondary Structure Modulates Translation of Tat-Dependent Formate Dehydrogenase N

G. Sawers, B. Berks, C. Punginelli, 2004, Journal of bacteriology.

Structural biology of Tat protein transport.

B. Berks, P. Stansfeld, S. Lea, 2014, Current opinion in structural biology.

An Essential Component of a Novel Bacterial Protein Export System with Homologues in Plastids and Mitochondria*

B. Berks, T. Palmer, F. Sargent, 1998, The Journal of Biological Chemistry.

The genetic basis of tetrathionate respiration in Salmonella typhimurium

G. Sawers, B. Berks, M. Hensel, 1999, Molecular microbiology.

Purification and characterization of a nitrous oxide reductase from Thiosphaera pantotropha. Implications for the mechanism of aerobic nitrous oxide reduction.

D. Richardson, B. Berks, J. Richardson, 1993, European journal of biochemistry.

Structural model for the protein-translocating element of the twin-arginine transport system

B. Berks, M. Sansom, J. Schnell, 2013, Proceedings of the National Academy of Sciences.

Crystal Structure of the Bacillus subtilis Phosphodiesterase PhoD Reveals an Iron and Calcium-containing Active Site

B. Berks, Steven Johnson, Fernanda Rodriguez, 2014, The Journal of Biological Chemistry.

New insights into the Tat protein transport cycle from characterizing the assembled Tat translocon

B. Berks, F. Alcock, 2022, Molecular microbiology.

In vivo experiments do not support the charge zipper model for Tat translocase assembly

B. Berks, Jesper Levring, F. Alcock, 2017, eLife.

Assembling the Tat protein translocase

B. Berks, P. Stansfeld, M. Wallace, 2016, eLife.

Subunit composition and in vivo substrate‐binding characteristics of Escherichia coli Tat protein complexes expressed at native levels

B. Berks, C. McDevitt, T. Palmer, 2006, The FEBS journal.

Regulation of the Hydrogenase-4 Operon of Escherichia coli by the σ54-Dependent Transcriptional Activators FhlA and HyfR

Yung-Sheng Chang, Frank Sargent, B. Berks, 2002, Journal of bacteriology.

Truncation Analysis of TatA and TatB Defines the Minimal Functional Units Required for Protein Translocation

B. Berks, T. Palmer, Philip A. Lee, 2002, Journal of bacteriology.

Constitutive Expression of Escherichia coli tat Genes Indicates an Important Role for the Twin-Arginine Translocase during Aerobic and Anaerobic Growth

G. Sawers, B. Berks, T. Palmer, 2001, Journal of bacteriology.

Structure of a proton-powered molecular motor that drives protein transport and gliding motility

B. Berks, S. Lea, J. Deme, 2020, bioRxiv.

Type 9 secretion system structures reveal a new protein transport mechanism

B. Berks, S. Lea, J. Deme, 2018, Nature.

The diversity of redox proteins involved in bacterial heterotrophic nitrification and aerobic denitrification.

Lisa C. Crossman, D. Richardson, B. Berks, 1998, Biochemical Society transactions.

Simplicity and complexity in electron transfer between NADH and c-type cytochromes in bacteria.

B. Berks, S. Ferguson, 1991, Biochemical Society Transactions.

Sequence analysis of subunits of the membrane‐bound nitrate reductase from a denitrifying bacterium: the integral membrane subunit provides a prototype for the dihaem electron‐carrying arm of a redox loop

D. Richardson, B. Berks, M. D. Page, 1995, Molecular microbiology.

Purified components of the Escherichia coli Tat protein transport system form a double-layered ring structure.

H. Saibil, B. Berks, U. Gohlke, 2001, European journal of biochemistry.

Oligomeric properties and signal peptide binding by Escherichia coli Tat protein transport complexes.

B. Berks, Matthias Müller, S. Carr, 2002, Journal of molecular biology.

Export of complex cofactor-containing proteins by the bacterial Tat pathway.

Frank Sargent, Tracy Palmer, B. Berks, 2005, Trends in microbiology.

Molecular dissection of TatC defines critical regions essential for protein transport and a TatB–TatC contact site

B. Berks, Matthias Müller, T. Palmer, 2012, Molecular microbiology.

Characterisation of the membrane‐extrinsic domain of the TatB component of the twin arginine protein translocase

B. Berks, T. Palmer, F. Sargent, 2011, FEBS letters.

Structures of the stator complex that drives rotation of the bacterial flagellum

B. Berks, P. Stansfeld, J. Coulton, 2020, bioRxiv.

Structures of the stator complex that drives rotation of the bacterial flagellum

B. Berks, P. Stansfeld, J. Coulton, 2020, Nature Microbiology.

Novel Phenotypes of Escherichia coli tat Mutants Revealed by Global Gene Expression and Phenotypic Analysis*

B. Berks, J. Hinton, I. Porcelli, 2004, Journal of Biological Chemistry.

Cysteine-scanning Mutagenesis and Disulfide Mapping Studies of the Conserved Domain of the Twin-arginine Translocase TatB Component*

B. Berks, M. Sansom, P. Bond, 2006, Journal of Biological Chemistry.

A naturally occurring bacterial Tat signal peptide lacking one of the ‘invariant’ arginine residues of the consensus targeting motif

B. Berks, T. Palmer, N. Stanley, 2001, FEBS letters.

Variable stoichiometry of the TatA component of the twin-arginine protein transport system observed by in vivo single-molecule imaging

R. Berry, M. Leake, B. Berks, 2008, Proceedings of the National Academy of Sciences.

Functional complexity of the twin‐arginine translocase TatC component revealed by site‐directed mutagenesis

B. Berks, T. Palmer, F. Sargent, 2002, Molecular microbiology.

A novel protein transport system involved in the biogenesis of bacterial electron transfer chains.

B. Berks, E. D. de Leeuw, T. Palmer, 2000, Biochimica et biophysica acta.

Novel heme ligation in a c-type cytochrome involved in thiosulfate oxidation: EPR and MCD of SoxAX from Rhodovulum sulfidophilum.

B. Berks, M. Cheesman, P. J. Little, 2001, Biochemistry.

Cysteine Scanning Mutagenesis and Disulfide Mapping Studies of the TatA Component of the Bacterial Twin Arginine Translocase*

B. Berks, I. Porcelli, T. Palmer, 2007, Journal of Biological Chemistry.

The Escherichia coli Cell Division Protein and Model Tat Substrate SufI (FtsP) Localizes to the Septal Ring and Has a Multicopper Oxidase-Like Structure

David S. Weiss, Pietro Roversi, Frank Sargent, 2009, Journal of molecular biology.

Positive Selection for Loss-of-Function tat Mutations Identifies Critical Residues Required for TatA Activity

G. Georgiou, B. Berks, T. Palmer, 2005, Journal of bacteriology.

Analysis of Tat targeting function and twin-arginine signal peptide activity in Escherichia coli.

B. Berks, T. Palmer, F. Sargent, 2010, Methods in molecular biology.

Path ¢ ndersandtrailblazers : a prokaryotic targetingsystemfor transportoffoldedproteins

B. Berks, T. Palmer, F. Sargent, 2005 .

Light traffic: photo-crosslinking a novel transport system.

B. Berks, T. Palmer, F. Sargent, 2004, Trends in biochemical sciences.

Assembly surprise for membrane proteins

B. Berks, 2022, Nature.

Mechanism of Thiosulfate Oxidation in the SoxA Family of Cysteine-ligated Cytochromes

B. Berks, Steven Johnson, S. Lea, 2015, The Journal of Biological Chemistry.

Structural analysis of substrate binding by the TatBC component of the twin-arginine protein transport system

Helen R Saibil, Tracy Palmer, Susan M Lea, 2009, Proceedings of the National Academy of Sciences.

The Tat protein translocation pathway and its role in microbial physiology.

B. Berks, T. Palmer, F. Sargent, 2003, Advances in microbial physiology.

Subunit Organization in the TatA Complex of the Twin Arginine Protein Translocase

B. Berks, A. Thomson, G. White, 2009, The Journal of Biological Chemistry.

In vivo experiments do not support the charge zipper model for Tat translocase assembly

B. Berks, Jesper Levring, F. Alcock, 2017, eLife.

Aberrant topologies of bacterial membrane proteins revealed by high sensitivity fluorescence labelling.

A. Kapanidis, B. Berks, Alfredas Bukys, 2023, Journal of molecular biology.

Targeting signals for a bacterial Sec‐independent export system direct plant thylakoid import by the ΔpH pathway

B. Berks, R. Klösgen, T. Palmer, 1998, FEBS letters.

Membrane interactions and self‐association of the TatA and TatB components of the twin‐arginine translocation pathway

B. Berks, I. Porcelli, E. D. de Leeuw, 2001, FEBS letters.

Genetic Evidence for a TatC Dimer at the Core of the Escherichia coli Twin Arginine (Tat) Protein Translocase

B. Berks, Matthias Müller, T. Palmer, 2011, Journal of Molecular Microbiology and Biotechnology.

Thiosulfate Reduction in Salmonella enterica Is Driven by the Proton Motive Force

B. Berks, G. Unden, M. Krehenbrink, 2011, Journal of bacteriology.

Structural insights into the mechanism of protein transport by the Type 9 Secretion System translocon

B. Berks, S. Lea, J. Deme, 2024, Nature microbiology.

Structural snapshots of the Type 9 protein translocon Plug-complex

B. Berks, S. Lea, J. Deme, 2018 .

A genetic screen for suppressors of Escherichia coli Tat signal peptide mutations establishes a critical role for the second arginine within the twin-arginine motif

Frank Sargent, Tracy Palmer, Grant Buchanan, 2001, Archives of Microbiology.